Domains of tobacco mosaic virus movement protein essential for its membrane association.
J Gen Virol
; 87(Pt 9): 2699-2707, 2006 Sep.
Article
en En
| MEDLINE
| ID: mdl-16894211
ABSTRACT
A series of deletion mutants of tobacco mosaic virus movement protein (TMV-MP) was used to identify domains of the protein necessary for membrane association. A membrane fraction was isolated from tobacco BY-2 protoplasts infected with wild-type and mutant TMV that produce MP carrying a 3 aa deletion. Deletions that affected membrane association were clustered around the two major hydrophobic regions of MP that are predicted to be transmembrane. Deletions in other hydrophobic regions also reduced membrane association. In addition, a non-functional mutant of MP, in which one of the known phosphorylation sites was eliminated, was not associated with cellular membranes, while a functional second site revertant restored membrane association. This indicates that MP function requires interaction with membrane; however, membrane association was not sufficient for function. Results are consistent with the hypothesis that TMV-MP is an integral or tightly associated membrane protein that includes two hydrophobic transmembrane domains.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Virus del Mosaico del Tabaco
/
Proteínas Virales
Tipo de estudio:
Risk_factors_studies
Idioma:
En
Revista:
J Gen Virol
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos